Gene interactions and pathways from curated databases and text-mining

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HIF1A — HSP90AA1

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Katschinski et al., J Biol Chem 2002 : Inhibition of the ATP dependent chaperone activity of HSP90 by novobiocin or geldanamycin prevented heat induced as well as hypoxia induced HIF-1alpha accumulation, indicating a common role of the HSP90 chaperone activity in HIF-1alpha stabilization by these two environmental parameters
Katschinski et al., Cell Physiol Biochem 2004 : Hypoxic accumulation of HIF-1alpha was delayed in a novel cell model deficient for HSP90beta as well as after treatment of wild-type cells with the HSP90 inhibitor geldanamycin, suggesting that HSP90 activity is involved in the rapid HIF-1alpha protein induction
Kubis et al., Biochim Biophys Acta 2005 (Anoxia) : We conclude that in skeletal muscle cells, HIF1alpha , in contrast to other tissues, may, in addition to its regulation by degradation, also be regulated by binding to HSP90 and subsequent inhibition of its import into the nuclei
Ono et al., J Cell Biochem 2006 : The inhibition of proteasome in the growth phase led to HIF-1alpha protein accumulation, whereas in the differentiation phase the inhibition of Hsp90 , which stabilizes HIF-1alpha, suppressed HIF-1alpha accumulation
Liu et al., Mol Cell 2007 : RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O ( 2 ) -independent and HSP90 inhibitor induced degradation of HIF-1alpha ... Inhibition of heat-shock protein 90 (HSP90) leads to O ( 2 ) /PHD/VHL independent degradation of HIF-1alpha
Liu et al., Cell cycle (Georgetown, Tex.) 2007 : Inhibitors of heat shock protein 90 (HSP90) dissociate HSP90 from HIF-1alpha and induce O2/PHD/VHL independent degradation of HIF-1alpha
Kim et al., Cancer Res 2009 (Carcinoma, Non-Small-Cell Lung...) : Inhibition of Hsp90 function by 17-allylamino-17-demethoxygeldanamycin or deguelin, a novel natural inhibitor of Hsp90, suppressed increases in HIF-1alpha/Hsp90 interaction and HIF-1alpha expression in radioresistant cells
van de Sluis et al., PloS one 2009 : Inhibition of HSP90 activity with 17-Allylamino-17-demethoxygeldanamycin ( 17-AAG ) increased COMMD1 mediated HIF-1alpha degradation independent of ubiquitin and pVHL
Zhang et al., Cancer Res 2010 : Further, decreased levels of endogenous Hsp90/Hsp70 proteins in JNK1-/- cells affected the protective roles of these chaperones in stabilizing newly synthesized HIF-1alpha, whereas enforced expression of Hsp90/Hsp70 in JNK1-/- cells increased HIF-1alpha stability relative to parental control cells